Literature DB >> 11124020

Conformational changes in the ribosome induced by translational miscoding agents.

O Jerinic1, S Joseph.   

Abstract

Ribosomes are dynamic complexes responsible for translating the genetic information encoded in mRNAs to proteins. The accuracy of this process is vital to the survival of an organism, and is often compromised by translational miscoding agents. Aminoglycosides are a group of miscoding agents that bind to the ribosome and reduce the fidelity of translation. Previous studies have shown that aminoglycosides alter the higher order structure of the ribosome. Here, we used a toeprinting assay to how that streptomycin, neomycin, kanamycin, gentamycin, and hygromycin B trigger conformational changes within Escherichia coli ribosome. Miscoding agents viomycin and 30% ethanol also cause similar structural changes within the ribosome. In contrast, antibiotics that do not cause miscoding, such as tetracycline, chloramphenicol, erythromycin, fusidic acid and spectinomycin, do not induce the conformational changes triggered by miscoding agents. Furthermore, ribosomes isolated from strains that are either streptomycin resistant or dependent for growth do not show these conformational changes in the presence of streptomycin. These results correlate structural changes in the ribosome induced by miscoding agents in vitro with their in vivo phenotype. Copyright 2000 Academic Press.

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Year:  2000        PMID: 11124020     DOI: 10.1006/jmbi.2000.4269

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  28 in total

1.  Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3.

Authors:  M Pioletti; F Schlünzen; J Harms; R Zarivach; M Glühmann; H Avila; A Bashan; H Bartels; T Auerbach; C Jacobi; T Hartsch; A Yonath; F Franceschi
Journal:  EMBO J       Date:  2001-04-17       Impact factor: 11.598

2.  EF-G-independent reactivity of a pre-translocation-state ribosome complex with the aminoacyl tRNA substrate puromycin supports an intermediate (hybrid) state of tRNA binding.

Authors:  Divya Sharma; Daniel R Southworth; Rachel Green
Journal:  RNA       Date:  2004-01       Impact factor: 4.942

Review 3.  Aminoglycoside antibiotics: structure, functions and effects on in vitro plant culture and genetic transformation protocols.

Authors:  I M G Padilla; L Burgos
Journal:  Plant Cell Rep       Date:  2010-07-20       Impact factor: 4.570

4.  Destabilization of the P site codon-anticodon helix results from movement of tRNA into the P/E hybrid state within the ribosome.

Authors:  Kevin G McGarry; Sarah E Walker; Huanyu Wang; Kurt Fredrick
Journal:  Mol Cell       Date:  2005-11-23       Impact factor: 17.970

5.  The hybrid state of tRNA binding is an authentic translation elongation intermediate.

Authors:  Silke Dorner; Julie L Brunelle; Divya Sharma; Rachel Green
Journal:  Nat Struct Mol Biol       Date:  2006-02-26       Impact factor: 15.369

6.  Reverse translocation of tRNA in the ribosome.

Authors:  Shinichiro Shoji; Sarah E Walker; Kurt Fredrick
Journal:  Mol Cell       Date:  2006-12-28       Impact factor: 17.970

7.  Recognition and positioning of mRNA in the ribosome by tRNAs with expanded anticodons.

Authors:  Sarah E Walker; Kurt Fredrick
Journal:  J Mol Biol       Date:  2006-05-17       Impact factor: 5.469

8.  Prolyl-tRNA(Pro) in the A-site of SecM-arrested ribosomes inhibits the recruitment of transfer-messenger RNA.

Authors:  Fernando Garza-Sánchez; Brian D Janssen; Christopher S Hayes
Journal:  J Biol Chem       Date:  2006-09-12       Impact factor: 5.157

9.  Elongation factor G stabilizes the hybrid-state conformation of the 70S ribosome.

Authors:  P Clint Spiegel; Dmitri N Ermolenko; Harry F Noller
Journal:  RNA       Date:  2007-07-13       Impact factor: 4.942

10.  Structural basis for hygromycin B inhibition of protein biosynthesis.

Authors:  Maria A Borovinskaya; Shinichiro Shoji; Kurt Fredrick; Jamie H D Cate
Journal:  RNA       Date:  2008-06-20       Impact factor: 4.942

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